A single-domain antibody (sdAb), also known as a nanobody, is an antibody fragment consisting of a single monomeric variable antibody domain. Like a whole antibody, it is able to bind selectively to a specific antigen. With a molecular weight of only 12–15 kDa, single-domain antibodies are much smaller than common antibodies which are composed of two heavy protein chains and two light chains, and even smaller than Fab fragments and single-chain variable fragments.
Pamela Jane Bjorkman NAS, AAAS is an American biochemist. She is the David Baltimore Professor of Biology and Biological Engineering at the California Institute of Technology (Caltech), Her research centers on the study of the three-dimensional structures of proteins related to Class I MHC, or Major Histocompatibility Complex, proteins of the immune system and proteins involved in the immune responses to viruses. Bjorkman is most well known as a pioneer in the field of structural biology.
Richard Henderson is a British molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.
In virology, a spike protein or peplomer protein is a protein that forms a large structure known as a spike or peplomer projecting from the surface of an enveloped virus. The proteins are usually glycoproteins that form dimers or trimers.
An ectodomain is the domain of a membrane protein that extends into the extracellular space. Ectodomains are usually the parts of proteins that initiate contact with surfaces, which leads to signal transduction. A notable example of an ectodomain is the S protein, commonly known as the spike protein, of the viral particle responsible for the COVID-19 pandemic. The ectodomain region of the spike protein (S) is essential for attachment and eventual entry of the viral protein into the host cell.
Kenneth Roux is an American academic biologist whose research addresses structural analysis of the AIDS viruses HIV-1 and SIV, and the antibodies that neutralize them, as well as food-allergen characterization and immunoassay development. He is the Kurt G. Hofer Professor of Biological Science at Florida State University (FSU), where he is affiliated with the Institute of Molecular Biophysics. He has been a member of FSU's biological science faculty since 1978. Roux received his B.S. degree from Delaware Valley College in 1970 and then attended Tulane University, from which he received his M.S. in 1972 and his Ph.D. in 1974.
Immunolabeling is a biochemical process that enables the detection and localization of an antigen to a particular site within a cell, tissue, or organ. Antigens are organic molecules, usually proteins, capable of binding to an antibody. These antigens can be visualized using a combination of antigen-specific antibody as well as a means of detection, called a tag, that is covalently linked to the antibody. If the immunolabeling process is meant to reveal information about a cell or its substructures, the process is called immunocytochemistry. Immunolabeling of larger structures is called immunohistochemistry.
Feline coronavirus (FCoV) is a positive-stranded RNA virus that infects cats worldwide. It is a coronavirus of the species Alphacoronavirus 1 which includes canine coronavirus (CCoV) and porcine transmissible gastroenteritis coronavirus (TGEV). It has two different forms: feline enteric coronavirus (FECV) that infects the intestines and feline infectious peritonitis virus (FIPV) that causes the disease feline infectious peritonitis (FIP).
Immunogold labeling or Immunogold staining (IGS) is a staining technique used in electron microscopy. This staining technique is an equivalent of the indirect immunofluorescence technique for visible light. Colloidal gold particles are most often attached to secondary antibodies which are in turn attached to primary antibodies designed to bind a specific antigen or other cell component. Gold is used for its high electron density which increases electron scatter to give high contrast 'dark spots'.
Betacoronavirus is one of four genera of coronaviruses. Member viruses are enveloped, positive-strand RNA viruses that infect mammals. The natural reservoir for betacoronaviruses are bats and rodents. Rodents are the reservoir for the subgenus Embecovirus, while bats are the reservoir for the other subgenera.
Kizzmekia "Kizzy" Shanta Corbett is an American viral immunologist. She is an Assistant Professor of Immunology and Infectious Diseases at Harvard T.H. Chan School of Public Health and the Shutzer Assistant Professor at the Harvard Radcliffe Institute since June 2021.
David Veesler is a French biochemist and an assistant professor in the Department of Biochemistry at the University of Washington, where his group focuses on the study the structural biology of infectious diseases. His team recently helped determine the structure of the SARS-CoV-2 spike glycoprotein using Cryo-EM techniques, and it is currently trying to identify neutralizing antibodies for SARS-CoV-2 that could be used as a preventative treatment against COVID-19 or as a post-exposure therapy using X-ray crystallography. Veesler is Howard Hughes Medical Investigators.
Jason S. McLellan is a structural biologist, professor in the Department of Molecular Biosciences and Robert A. Welch Chair in Chemistry at The University of Texas at Austin who specializes in understanding the structure and function of viral proteins, including those of coronaviruses. His research focuses on applying structural information to the rational design of vaccines and other therapies for viruses, including SARS-CoV-2, the novel coronavirus that causes COVID-19. McLellan and his team collaborated with researchers at the National Institute of Allergy and Infectious Diseases’ Vaccine Research Center to design a stabilized version of the SARS-CoV-2 spike protein, which biotechnology company Moderna used as the basis for the vaccine mRNA-1273, the first COVID-19 vaccine candidate to enter phase I clinical trials in the U.S. At least three other vaccines use this modified spike protein: those from Pfizer and BioNTech; Johnson & Johnson and Janssen Pharmaceuticals; and Novavax.
Iota variant, also known as lineage B.1.526, is one of the variants of SARS-CoV-2, the virus that causes COVID-19. It was first detected in New York City in November 2020. The variant has appeared with two notable mutations: the E484K spike mutation, which may help the virus evade antibodies, and the S477N mutation, which may help the virus bind more tightly to human cells.
The membrane (M) protein is an integral membrane protein that is the most abundant of the four major structural proteins found in coronaviruses. The M protein organizes the assembly of coronavirus virions through protein-protein interactions with other M protein molecules as well as with the other three structural proteins, the envelope (E), spike (S), and nucleocapsid (N) proteins.
Spike (S) glycoprotein is the largest of the four major structural proteins found in coronaviruses. The spike protein assembles into trimers that form large structures, called spikes or peplomers, that project from the surface of the virion. The distinctive appearance of these spikes when visualized using negative stain transmission electron microscopy, "recalling the solar corona", gives the virus family its main name.
Jesse D. Bloom is an American computational virologist and Professor in the Basic Sciences Division, the Public Health Sciences Division, and the Herbold Computational Biology Program, at the Fred Hutchinson Cancer Center. He is also an Investigator of the Howard Hughes Medical Institute, and an Affiliate Professor in the University of Washington departments of Genome Sciences and Microbiology.
Julie Biteen is a Canadian-born American chemist who is professor of chemistry and biophysics at the University of Michigan. Her research considers the development of imaging systems for biological systems. She was named the Stanford University Sessler Distinguished Alumni Lecturer in 2021.
Deborah F. Kelly is an American biomedical engineer who is a professor at Pennsylvania State University. Her research makes use of cryogenic electron microscopy to better understand human development and disease. She serves as President of the Microscopy Society of America.
